Abstract
The thermodynamics of the hydrophobic effect, as measured primarily through the temperature dependence of solubility, is reviewed, and then a class of models that incorporate the basic mechanism of hydrophobicity is described. These models predict a quantitative relation between the free energy of hydrophobic hydration and the strength of the solvent-mediated attraction between pairs of solute molecules. It is remarked that the free energy of attraction being just of the order of the thermal energy kT may be important for the effective operation of the hydrophobic effect in proteins. Deviations from pairwise additivity of hydrophobic forces are also briefly discussed.
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